ID G1SRL9_RABIT Unreviewed; 2502 AA.
AC G1SRL9;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 11-DEC-2019, sequence version 3.
DT 27-MAR-2024, entry version 79.
DE SubName: Full=Myosin XVIIIB {ECO:0000313|Ensembl:ENSOCUP00000005831.4};
GN Name=MYO18B {ECO:0000313|Ensembl:ENSOCUP00000005831.4};
OS Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986 {ECO:0000313|Ensembl:ENSOCUP00000005831.4, ECO:0000313|Proteomes:UP000001811};
RN [1] {ECO:0000313|Ensembl:ENSOCUP00000005831.4, ECO:0000313|Proteomes:UP000001811}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Thorbecke {ECO:0000313|Proteomes:UP000001811};
RX PubMed=21993624; DOI=10.1038/nature10530;
RA Lindblad-Toh K., Garber M., Zuk O., Lin M.F., Parker B.J., Washietl S.,
RA Kheradpour P., Ernst J., Jordan G., Mauceli E., Ward L.D., Lowe C.B.,
RA Holloway A.K., Clamp M., Gnerre S., Alfoldi J., Beal K., Chang J.,
RA Clawson H., Cuff J., Di Palma F., Fitzgerald S., Flicek P., Guttman M.,
RA Hubisz M.J., Jaffe D.B., Jungreis I., Kent W.J., Kostka D., Lara M.,
RA Martins A.L., Massingham T., Moltke I., Raney B.J., Rasmussen M.D.,
RA Robinson J., Stark A., Vilella A.J., Wen J., Xie X., Zody M.C., Baldwin J.,
RA Bloom T., Chin C.W., Heiman D., Nicol R., Nusbaum C., Young S.,
RA Wilkinson J., Worley K.C., Kovar C.L., Muzny D.M., Gibbs R.A., Cree A.,
RA Dihn H.H., Fowler G., Jhangiani S., Joshi V., Lee S., Lewis L.R.,
RA Nazareth L.V., Okwuonu G., Santibanez J., Warren W.C., Mardis E.R.,
RA Weinstock G.M., Wilson R.K., Delehaunty K., Dooling D., Fronik C.,
RA Fulton L., Fulton B., Graves T., Minx P., Sodergren E., Birney E.,
RA Margulies E.H., Herrero J., Green E.D., Haussler D., Siepel A., Goldman N.,
RA Pollard K.S., Pedersen J.S., Lander E.S., Kellis M.;
RT "A high-resolution map of human evolutionary constraint using 29 mammals.";
RL Nature 478:476-482(2011).
RN [2] {ECO:0000313|Ensembl:ENSOCUP00000005831.4}
RP IDENTIFICATION.
RC STRAIN=Thorbecke {ECO:0000313|Ensembl:ENSOCUP00000005831.4};
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Myosin family. {ECO:0000256|ARBA:ARBA00008314,
CC ECO:0000256|PROSITE-ProRule:PRU00782}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00782}.
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DR SMR; G1SRL9; -.
DR STRING; 9986.ENSOCUP00000005831; -.
DR PaxDb; 9986-ENSOCUP00000005831; -.
DR Ensembl; ENSOCUT00000006743.4; ENSOCUP00000005831.4; ENSOCUG00000006734.4.
DR eggNOG; KOG0161; Eukaryota.
DR GeneTree; ENSGT00940000158067; -.
DR HOGENOM; CLU_000192_1_1_1; -.
DR InParanoid; G1SRL9; -.
DR TreeFam; TF339614; -.
DR Proteomes; UP000001811; Unplaced.
DR Bgee; ENSOCUG00000006734; Expressed in skeletal muscle tissue and 9 other cell types or tissues.
DR GO; GO:0031941; C:filamentous actin; IEA:Ensembl.
DR GO; GO:0016461; C:unconventional myosin complex; IEA:Ensembl.
DR GO; GO:0030018; C:Z disc; IEA:Ensembl.
DR GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003774; F:cytoskeletal motor activity; IEA:UniProtKB-UniRule.
DR GO; GO:0055013; P:cardiac muscle cell development; IEA:Ensembl.
DR GO; GO:0001701; P:in utero embryonic development; IEA:Ensembl.
DR GO; GO:0001570; P:vasculogenesis; IEA:Ensembl.
DR CDD; cd01386; MYSc_Myo18; 1.
DR Gene3D; 1.10.10.820; -; 1.
DR Gene3D; 1.20.58.530; -; 1.
DR Gene3D; 6.20.240.20; -; 1.
DR Gene3D; 3.40.850.10; Kinesin motor domain; 1.
DR Gene3D; 1.20.120.720; Myosin VI head, motor domain, U50 subdomain; 1.
DR Gene3D; 4.10.270.10; Myosin, subunit A; 1.
DR InterPro; IPR000048; IQ_motif_EF-hand-BS.
DR InterPro; IPR036961; Kinesin_motor_dom_sf.
DR InterPro; IPR001609; Myosin_head_motor_dom.
DR InterPro; IPR036064; MYSc_Myo18.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR45615; MYOSIN HEAVY CHAIN, NON-MUSCLE; 1.
DR PANTHER; PTHR45615:SF8; UNCONVENTIONAL MYOSIN-XVIIIB; 1.
DR Pfam; PF00063; Myosin_head; 1.
DR PRINTS; PR00193; MYOSINHEAVY.
DR SMART; SM00242; MYSc; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF57997; Tropomyosin; 1.
DR PROSITE; PS50096; IQ; 1.
DR PROSITE; PS51456; MYOSIN_MOTOR; 1.
PE 3: Inferred from homology;
KW Actin-binding {ECO:0000256|PROSITE-ProRule:PRU00782};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU00782}; Coiled coil {ECO:0000256|SAM:Coils};
KW Motor protein {ECO:0000256|ARBA:ARBA00023175, ECO:0000256|PROSITE-
KW ProRule:PRU00782};
KW Myosin {ECO:0000256|ARBA:ARBA00023123, ECO:0000256|PROSITE-
KW ProRule:PRU00782};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00782}; Reference proteome {ECO:0000313|Proteomes:UP000001811}.
FT DOMAIN 502..1267
FT /note="Myosin motor"
FT /evidence="ECO:0000259|PROSITE:PS51456"
FT REGION 1..475
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1143..1166
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2073..2181
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2218..2252
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2390..2414
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2427..2502
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1335..1609
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1634..1712
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1764..1892
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1955..2017
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 41..63
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 77..108
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 311..331
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2073..2089
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2093..2117
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2152..2166
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2440..2456
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2474..2497
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 593..600
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
SQ SEQUENCE 2502 AA; 275193 MW; C7E51241EE94A37A CRC64;
MAISSRLALW EQKIREEDKS PPPSSPPPLF SVIPGGFIRQ LVRETEKESK EARRRKEAAL
ASPERETPEA PIAQPRSKSG SDGQPGGPPL SQDSPARSPQ SADVPAQGSQ GAGSPDPVLM
TSINGEKPQE PGPSRTPAKK PFKRGVRRGD VLLMVAKLDP EAAKPQDAPP PATDPGGGRK
AGSPGTPCGP QADTKDLAPK AEKTWTGVLG EPGQGTKGER GQGPMGKGAG GPQTKGPKAG
EPQGKEGQGT KPQAQGDRAR PGTTEKEGGD PPSKTAKGTL SKDAGGQEKV AGPPVQARKW
GGALGRRGQW DGVQSRKDKA GKVEKAAGPQ TKAEKTGEVQ RAMGKGEEEA SRVAQQAGGP
PQELGKGVRA PSTSGEAGMA EKHCEAAKDV VTRGEWPGAA GKKGRPQSPG QATEEPRARA
EEDGAEALQV EPEAAGRPGL ETSVPRPPTL KETQEGPALQ EAGGGGWSGD LDQAPGDRWY
EAEKVWLVRK DGFTLANPPE LDQAEDLASL VSVSESSVLH TLLQRHRARL PHTCSGPDLI
VLQPQGPSAP STGKVPVPRG RWDRSPAHVA SLAQRAYWAL LSQRRDQSVV ALGRSGSGKT
TCCEQVLEHL LAMAGSVDGR VSAEKIRATF TVLRAFGCAS TGHGRSATRF AMVMALDFNA
TGRVTAAQLQ TALLETSRVA RRPAGEGSFH VFSQMLAGLD LDLRTELHLH QLAASSSFGL
GVWAKPEEKQ KAAAAFAQLQ GAMETLGISA SEQQAIWRVL AAIYHLGAAG ACKVGRKQFM
RFEWANHAAE ALGCEYEELN TATFKHHLRQ IIEQVTSRPS RRGLEDEETS SGLKMTGVEC
VEGMASGLYQ ELFAAVVSLI NRSFSSHHLS MGSIMVVDSP GFQSPRHEGK ERAATFEELC
HNYVHERLQL LYYQRTFVST LERHREEGVP VQFDLPERSP ATSVAVVDQS PSQQVPLAAG
GGAEDAGGLF WVLDEEVRVE GSSDSVVLER LCAAFEKKGA GAEGTSALRA CEQPLQCEIF
HQLGHDPVRY DLTGWLHRAK PNLAALDAPQ VLQQSKREEL RNLFQARAKL PAVCRTVAGL
EGTSQQALQR SRVLRRTFAS RLAAVRRRAP CSQIQLQTDA LINVIRRSHL HFIHCLAPTP
LLESRTGQGS PTPPQPGGDE TKAGGPPALD IPALRVQLAG SHIMEALRLH RAGYADHMGL
TQFRRRFQVL DPPLLKKLVL ASEGVDERKA VEELLQSLDL GKKAVALGHS QVFLKAGVVS
RLEKQREKLV SQSIILFQAA CKGFLSRQEF KKLKIRRLAA RSIQRNMAVF LAVKDWPWWR
LLGSLRPLLS SSIGSEQLRA KEEELTALRH KLEKSEKLRN ELRQNTDVLE SKIADLTTEL
ADERFKGDVA CQVLESEWAE RLQASRELQE LKSKYEQVQK KLGEVEKQLE EAQQKIQLSD
LERNRPGGAD EWQMRLDCAQ MENEFLRKRL QQCEERLDSE LTARKELEQK LGELQGAYEG
ARKAAQQLKR KCHHLTCDLE DTRVLLENQQ SRNHELEKKQ KKFDMQLAQA LGESVFEKSL
REKVTQENTS VRWELGQLQQ QLQKKEQEAS QLKQEVEILQ DQKRELLGSS SMGEDCVAAL
KERLWKLESS ALEQQKIQGQ QESTIKQLEQ LRQQFELEIE RMQQMYQKDR EDKEEELEDV
RQSCQKRLRQ LEMQLEQEYE EKQMALHEKQ DLEGLIGTLC EQIGHRDFDV EKRLRRDLRR
THALLSDVQL LLGTMEDGKT SVSKEELEKV HSQLEQSEAK CEDALKTQKA LTADLETMHS
ELENMTRNKS LVDEQLYRLQ FERADLLKRI DEDQDDLNEL MQKHKDLIAQ SASDIGQIQE
LQQQLEEAKK EKHKLQEQLQ VAQMRVEYLE QSTVDRAIVS RQEAVICDLE NKTEFQKVQI
KRFEVLVIRL RDSLIKMGEE LSRAAASEAQ QRESSQYYQR RLEELKAEME ELVQREAEAG
RRCVELEKYV EELAAVRQTL QTDLETSIRR IADLQAALEE VASSDSDTES VQTAVDCGAG
GQRELDNVSV ISSQPEGSLQ SWSSCTLSLA ADTMRSPSRL STISSRIPSP RMSEEAGDAE
RPRPASALSR AWDDRGKTPG ETSLSPGSVR RHKSCHFGDG EGVGAQRKAT ERSGALSASL
ASRSPDTSPL PRAKLPSPSA ALSEFVEGLR RKRAQKGPGS RLGLEDWPTL PIYQTTGAST
LRRGRAGSDE GDLSLRAGGI SPLETEGAAG TSAGLLRSTS LRCIPSEGAQ GTAMLPEQRK
TRFSSCEALL ESGPGSWRRL SPSTAPGGML LSPPLRPRRR CLEASVDDAG CPDLGKEPLV
FQNRQFAHLM EEPLDSDPGS WKTPSLHYER KTKVDFDEFL PAIRKPGAST SLVRASKDGA
SGPQAPSVHF ETEDADRGFL SGIKTILKKS PEPREDPAHL SDSSSSSSSI VSYKSADSIK
SRPGLPRLQG DGGERTSPES REPVPGRRED DVESIMKKYL QK
//
